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New approach to capture and characterize synaptic proteome.


ABSTRACT: Little is known regarding the identity of the population of proteins that are transported and localized to synapses. Here we describe a new approach that involves the isolation and systematic proteomic characterization of molecular motor kinesins to identify the populations of proteins transported to synapses. We used this approach to identify and compare proteins transported to synapses by kinesin (Kif) complexes Kif5C and Kif3A in the mouse hippocampus and prefrontal cortex. Approximately 40-50% of the protein cargos identified in our proteomics analysis of kinesin complexes are known synaptic proteins. We also found that the identity of kinesins and where they are expressed determine what proteins they transport. Our results reveal a previously unappreciated role of kinesins in regulating the composition of synaptic proteome.

SUBMITTER: Liu XA 

PROVIDER: S-EPMC4234550 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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New approach to capture and characterize synaptic proteome.

Liu Xin-An XA   Kadakkuzha Beena B   Pascal Bruce B   Steckler Caitlin C   Akhmedov Komolitdin K   Yan Long L   Chalmers Michael M   Puthanveettil Sathyanarayanan V SV  

Proceedings of the National Academy of Sciences of the United States of America 20141028 45


Little is known regarding the identity of the population of proteins that are transported and localized to synapses. Here we describe a new approach that involves the isolation and systematic proteomic characterization of molecular motor kinesins to identify the populations of proteins transported to synapses. We used this approach to identify and compare proteins transported to synapses by kinesin (Kif) complexes Kif5C and Kif3A in the mouse hippocampus and prefrontal cortex. Approximately 40-5  ...[more]

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